OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools
Morgan Dasovich, Anthony K. L. Leung
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1552-1572
Open Access | Times Cited: 34

Showing 1-25 of 34 citing articles:

ADP-ribosylation from molecular mechanisms to therapeutic implications
Marcin J. Suskiewicz, Evgeniia Prokhorova, J.G.M. Rack, et al.
Cell (2023) Vol. 186, Iss. 21, pp. 4475-4495
Open Access | Times Cited: 72

ADP-ribose contributions to genome stability and PARP enzyme trapping on sites of DNA damage; paradigm shifts for a coming-of-age modification
Élise Rouleau-Turcotte, John M. Pascal
Journal of Biological Chemistry (2023) Vol. 299, Iss. 12, pp. 105397-105397
Open Access | Times Cited: 24

Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG
Edoardo José Longarini, Ivan Matić
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 15

PARPs and ADP-ribosylation-mediated biomolecular condensates: determinants, dynamics, and disease implications
Hongrui Liu, Meenakshi Pillai, Anthony K. L. Leung
Trends in Biochemical Sciences (2025)
Closed Access | Times Cited: 1

The Mac1 ADP-ribosylhydrolase is a Therapeutic Target for SARS-CoV-2
Rahul K. Suryawanshi, Priyadarshini Jaishankar, G.J. Correy, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 5

Cation-induced intramolecular coil-to-globule transition in poly(ADP-ribose)
Tong Wang, Kush Coshic, Mohsen Badiee, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 4

Poly ADP-Ribosylation in a Plant Pathogenic Oomycete Phytophthora infestans: A Key Controller of Growth and Host Plant Colonisation
Viktoriya O. Samarskaya, Sofya Koblova, Tatiana Suprunova, et al.
Journal of Fungi (2025) Vol. 11, Iss. 1, pp. 29-29
Open Access

The Mac1 ADP-ribosylhydrolase is a Therapeutic Target for SARS-CoV-2
Rahul K. Suryawanshi, Priyadarshini Jaishankar, G.J. Correy, et al.
(2025)
Open Access

The Mac1 ADP-ribosylhydrolase is a Therapeutic Target for SARS-CoV-2
Rahul K. Suryawanshi, Priyadarshini Jaishankar, G.J. Correy, et al.
(2025)
Open Access

Regulation of stress granule maturation and dynamics by poly(ADP-ribose) interaction with PARP13
Shang-Jung Cheng, Temitope Gafaar, Jijin R. A. Kuttiyatveetil, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access

Discovery of reversing enzymes for RNA ADP-ribosylation reveals a possible defence module against toxic attack
Yang Lu, M. Schuller, Nathan P. Bullen, et al.
Nucleic Acids Research (2025) Vol. 53, Iss. 4
Open Access

dELTA-MS: A Mass Spectrometry-Based Proteomics Approach for Identifying ADP-Ribosylation Sites and Forms
Isabel Uribe, Emily Zahn, Richard Searfoss, et al.
Journal of Proteome Research (2025)
Closed Access

Supplementation with NAD+ and its precursors: A rescue of female reproductive diseases
Lan Li, Xin Zhou, Liu Wen-e, et al.
Biochemistry and Biophysics Reports (2024) Vol. 38, pp. 101715-101715
Open Access | Times Cited: 2

USP14 inhibition promotes DNA damage repair and represses ovarian granulosa cell senescence in premature ovarian insufficiency
Linzi Ma, Ao Wang, Yun-Hui Lai, et al.
Journal of Translational Medicine (2024) Vol. 22, Iss. 1
Open Access | Times Cited: 2

Privileged Scaffolds for Potent and Specific Inhibitors of Mono-ADP-Ribosylating PARPs
Maria Giulia Nizi, Chiara Sarnari, Oriana Tabarrini
Molecules (2023) Vol. 28, Iss. 15, pp. 5849-5849
Open Access | Times Cited: 4

PARP7 Inhibition: A Promising Pathway to Advancements in Cancer Therapy
Robert B. Kargbo
ACS Medicinal Chemistry Letters (2023) Vol. 14, Iss. 9, pp. 1141-1143
Open Access | Times Cited: 4

Interferon-Induced PARP14-Mediated ADP-Ribosylation in p62 Bodies Requires an Active Ubiquitin-Proteasome System
Rameez Raja, Banhi Biswas, Rachy Abraham, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

An E3 ubiquitin ligase localization screen uncovers DTX2 as a novel ADP-ribosylation-dependent regulator of DNA double-strand break repair
Billel Djerir, Isabelle Marois, Jean-Christophe Dubois, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 8, pp. 107545-107545
Open Access | Times Cited: 1

Pathological and physiological roles of ADP-ribosylation: established functions and new insights
Karla L. H. Feijs, Nonso Josephat Ikenga, Roko Žaja
Biological Chemistry (2024) Vol. 405, Iss. 9-10, pp. 567-581
Closed Access | Times Cited: 1

PARP15 is a Susceptibility Locus for Clarkson Disease (Monoclonal Gammopathy–Associated Systemic Capillary Leak Syndrome)
Eunice C. Chan, Ararat J. Ablooglu, Chandra C. Ghosh, et al.
Arteriosclerosis Thrombosis and Vascular Biology (2024) Vol. 44, Iss. 12, pp. 2628-2646
Closed Access | Times Cited: 1

Molecular tools unveil distinct waves of ADP-ribosylation during DNA repair
Morgan Dasovich, Anthony K. L. Leung
Cell Reports Methods (2023) Vol. 3, Iss. 5, pp. 100484-100484
Open Access | Times Cited: 3

A chemical biology/modular antibody platform for ADP-ribosylation signaling
Helen Dauben, Edoardo José Longarini, Ivan Matić
Trends in Biochemical Sciences (2023) Vol. 48, Iss. 10, pp. 910-911
Open Access | Times Cited: 2

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